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  • 1980-1984  (2)
  • 1
    ISSN: 1432-0428
    Keywords: Insulin receptor ; obesity ; adipocyte ; subcutaneous fat ; omental fat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The insulin binding properties and the molecular weights of the insulin receptor and its insulin binding subunit were studied in omental and subcutaneous adipocytes prepared from obese- and normal-weight subjects. Insulin binding by such adipocytes was decreased in obesity when the binding activity was expressed per unit of cell surface area. No significant difference from the lean controls was evident, however, when binding was calculated on a per cell basis, indicating that the total receptor content of the cells from the obese subjects was not altered. In addition, the normal difference in the receptor binding affinities previously reported between omental and subcutaneous cells from lean individuals was unaffected by the obese condition. Studies of the molecular weight of the non-reduced insulin receptor in fat cell membranes prepared from pieces of omental and subcutaneous fat demonstrated a major receptor species of 390–425K Mr. In contrast, adipocytes isolated by collagenase treatment of the fat had heterogenous non-reduced receptor species of Mr 355K, 285K and small amounts of 427K and 182K. Although different non-reduced receptor species were evident depending on the adipocyte receptor preparation (e.g. isolated adipocytes or fat cell membranes), no differences were found between obese and lean controls or between subcutaneous and omental receptors when the appropriate comparisons were made. Upon sulphydryl reduction, all receptor preparations had a major binding subunit of 125K Mr. In conclusion, obesity is characterized by a dilution of the insulin receptor over the adipocyte cell surface in the absence of a change in total cellular content of receptors. The difference in insulin binding affinities between omental and subcutaneous adipocytes could not be explained by an alteration in receptor molecular weight.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Affinity partitioning in dextran-polyethylene glycol-water biphasic systems has demonstrated that myosin has hydrophobic surface properties. In 0.5 M KCl at pH 7.5 myosin is transferred at increasing amounts to the polyethylene glycol-rich upper phase when an increasing proportion of that polymer in the system is replaced by its ester with lauric, myristic or palmitic acid. This shows that on its surface myosin has binding sites with affinity for long chain fatty acyl groups. Partition studies on the ionic strength range of 0.2–0.6 M KCl at pH 7.5 at 4°C and 20°C, respectively, in systems containing polyethylene glycol-palmitate showed that the affinity of myosin for the palmitate group becomes greater with (1) an increase in ionic strength, and (2) an increase in temperature at constant ionic strength. The affinity of myosin for the palmitate group also increases with a decrease in the pH in the range of 5.6 8.5. The increase in the affinity of myosin for the palmitate group parallels the increase in the tendency of myosin to self-interact and yield filaments.
    Type of Medium: Electronic Resource
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